ID A0A1M3R1K1_9SPHI Unreviewed; 673 AA.
AC A0A1M3R1K1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=BGP13_10965 {ECO:0000313|EMBL:OJY98162.1};
OS Sphingobacteriales bacterium 40-81.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895835 {ECO:0000313|EMBL:OJY98162.1, ECO:0000313|Proteomes:UP000184064};
RN [1] {ECO:0000313|EMBL:OJY98162.1, ECO:0000313|Proteomes:UP000184064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=40-81 {ECO:0000313|EMBL:OJY98162.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJY98162.1}.
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DR EMBL; MKWF01000010; OJY98162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3R1K1; -.
DR STRING; 1895835.BGP13_10965; -.
DR Proteomes; UP000184064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00357; CSP; 2.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 564..646
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 654..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 76770 MW; 47247215732E600A CRC64;
MGRKNSKNTK SKTSHGILTG TLDVTRSGIG YVIVENREKD IFIRPQDFNH ALHGDRVSVK
ITREGRSGRM EGEITEVVER KQSEFVGRLE LNKDFGFFIP DKAKGTPDMY IPGDKTNGAK
NGDRVVVRIT EWNSRDRSPN GEVISILNAG DENDMAMKEI LVDAGFELDF DDDALEEAAR
IPDAIPASEI KKRKDMRDIF TITIDPVDAK DFDDAISYRK LKNGVYEIGV HIADVSYYIE
PDTPLDKNAY QRATSVYLPD RVLPMLPEHI SNVLCSLRPK EEKLTFSAIF QINAKGEVKS
HWLGRTIIYS DHRFTYEEVQ EIIEKKEGLY KDEVLFLNDL AQKFRRQRFK NGAINFSSQE
VRFKLDENGK PVGIVVKESK EAHQLIEEFM LLANRTVAED VAKVKVNKHP LPFPYRVHDT
PDEEKLLPFV DFAKKFGHKF DTKSPEGIAA SFNKMLAEVQ GKPEQHVLEQ LGIRTMAKAV
YTKDNIGHYG LGFEHYCHFT SPIRRYPDIL VHRILQEVLD GKMNPDKKME EKCRHSSERE
RAAMDAERAA NKYKQVEFMQ DYIGDEFEGV ISGVAGFGFW VETVAHKCEG LVSIQSLLDY
DDFRLIESEY CLAGRRSGRT FRMGDKVWIK VIAANLGKRQ LDYEWVIKPG DIAANGTAQQ
KPSSKKTKKG KRK
//
